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06
Feb
Trypsin: Activation, Catalytic Mechanism, and Applications
Technical Insights & Laboratory Best Practices
Trypsin is a key serine protease involved in protein digestion. After activation in the small intestine, it specifically cleaves peptide bonds on the carboxyl side of lysine (Lys) and arginine (Arg) residues, facilitating nutrient absorption.
I. Activation Process
1. Zymogen Secretion
Synthesized by the pancreas as trypsinogen (inactive form) to prevent premature tissue damage.
2. Enteropeptidase Trigger
In the small intestine, enteropeptidase (enterokinase) cleaves trypsinogen into active trypsin.
Note: Activated trypsin initiates an autocatalytic cascade, rapidly activating more trypsinogen and other digestive enzymes.
II. Catalytic Mechanism
1. Specific Peptide Bond Cleavage
Trypsin exhibits high substrate specificity, hydrolyzing peptide bonds at the C-terminal side of Lys or Arg. This precision makes it a fundamental tool for degrading large protein substrates into smaller peptides.
2. The Central Regulator
Trypsin acts as the "master switch" for pancreatic enzymes, activating:
- ✔ Chymotrypsinogen → Chymotrypsin
- ✔ Procarboxypeptidase → Carboxypeptidase
- ✔ Proelastase → Elastase
III. Key Functional Characteristics
| Feature | Description |
|---|---|
| Calcium Dependence | Ca2+ ions stabilize the structure and prevent autolytic degradation. |
| Autolysis Risk | Susceptible to self-digestion at suboptimal pH (especially pH > 9.0). |
| pH Optimum | Typically exhibits peak activity around pH 7.5–8.5. |
IV. Clinical Significance
- High Activity: Associated with pancreatitis or pancreatic carcinoma.
- Low Activity: Linked to malabsorption and cystic fibrosis.
V. Industrial Applications
Cell Culture: Essential for dissociating adherent cells by cleaving adhesion proteins.
Medical: Used in wound debridement to remove necrotic tissue and accelerate healing.
Biofargo team
